ID A0A0N0SYR4_9ACTN Unreviewed; 321 AA.
AC A0A0N0SYR4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:KOV62298.1};
GN ORFNames=ADK64_24745 {ECO:0000313|EMBL:KOV62298.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV62298.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOV62298.1}.
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DR EMBL; LGDV01000199; KOV62298.1; -; Genomic_DNA.
DR RefSeq; WP_053662007.1; NZ_LGDV01000199.1.
DR AlphaFoldDB; A0A0N0SYR4; -.
DR STRING; 1415544.ADK64_24745; -.
DR PATRIC; fig|1415544.3.peg.5311; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000037687; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KOV62298.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037687}.
FT DOMAIN 12..242
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 321 AA; 35305 MW; 3AEB1FE1181EC9D9 CRC64;
MTTPVNRLRP RRSCLAVPGS NPRFLEKAQG LPADQVFLDL EDACAPLAKP EARHTIVKFL
NEGDWTGKTR VVRVNDWTTE WTYRDVVTVV EGAGQNLDCI MLPKVQTAEQ IVALDLLLTQ
IEKTMGFEVG KIGIEAQIEN AQGLNNVNEI ATASQRVETI IFGPADFMAS INMKSLVVGE
QPPGYPADAY HYILMKILMA ARANNLQAID GPYLQIRNID GYREVAQRAA ALGFDGKWVL
HPGQVEASNE IFSPSQEDYD HAELILDAYD YYTSEAGGKK GSAMLGDEMI DEASRKMALV
VSGKGRAAGM QRTSKFEIPE A
//